EC Number   |
Cofactor |
Reference |
|---|
   1.1.3.38 | 8alpha-(N3-Histidyl)-FAD |
covalently bound prosthetic group |
10674 |
| 1.1.3.38 | 8alpha-(N3-Histidyl)-FAD |
the octamer contains 1 mol of covalently-bound flavin per mol of subunit |
10666 |
| 1.1.3.38 | FAD |
- |
655977, 740440, 762649, 763609 |
| 1.1.3.38 | FAD |
a 8alpha-histidyl-C6-cysteinyl bound FAD, vanillyl-alcohol oxidase contains a covalently alpha-histidyl bound FAD, which represents the most frequently encountered covalent flavin-protein linkage, autocatalytic incorporation mechanism, overview. Incubation of recombinant apoVAO with FAD results in full restoration of enzyme activity dependent on FAD concentration, displaying a hyperbolic relationship with KFAD = 0.0023 mM, kactivation = 0.13/min. Formation of the covalent flavin-protein bond is an autocatalytic process, which proceeds via a reduced flavin intermediate, overview |
697878 |
| 1.1.3.38 | FAD |
although mutations H422A, H422T or H422C, prevents covalent linkage of FAD, mutant enzymes contains tightly bound FAD. Covalent histidyl-FAD bond is not essential for FAD binding |
655975 |
| 1.1.3.38 | FAD |
covalently bound |
10673, 656076 |
| 1.1.3.38 | FAD |
covalently bound FAD |
763252 |
| 1.1.3.38 | FAD |
covalently bound in wild-type enzyme and mutant enzymes D170E and D170S, 50% of the FAD is covalently bound in mutant enzyme D170A and no FAD is covalently bound in mutant enzyme D170N |
654161 |
| 1.1.3.38 | FAD |
covalently bound. Covalent flavinylation is an autocatalytical process in which His61 plays a crucial role by activating His422 |
655990 |
| 1.1.3.38 | FAD |
eugenol oxidase is partly expressed in the apo form, but can be fully flavinylated by the addition of FAD. FAD is covalently linked to residue H390. Protein shows absorption maxima at 365 nm and 441 nm, and shoulders at 313 nm, 394 nm, and 461 nm |
763010 |
